David D Boehr

Summary

Affiliation: Pennsylvania State University
Country: USA

Publications

  1. pmc Long-range interaction networks in the function and fidelity of poliovirus RNA-dependent RNA polymerase studied by nuclear magnetic resonance
    Xiaorong Yang
    Department of Chemistry, The Pennsylvania State University, University Park, PA 16802, USA
    Biochemistry 49:9361-71. 2010
  2. doi request reprint Promiscuity in protein-RNA interactions: conformational ensembles facilitate molecular recognition in the spliceosome: conformational diversity in U2AF⁶⁵ facilitates binding to diverse RNA sequences
    David D Boehr
    Department of Chemistry, The Pennsylvania State University, 240 Chemistry Building, University Park, PA, USA
    Bioessays 34:174-80. 2012
  3. pmc The role of dynamic conformational ensembles in biomolecular recognition
    David D Boehr
    Department of Chemistry, The Pennsylvania State University, University Park, Pennsylvania, USA
    Nat Chem Biol 5:789-96. 2009
  4. pmc Motif D of viral RNA-dependent RNA polymerases determines efficiency and fidelity of nucleotide addition
    Xiaorong Yang
    Department of Chemistry, The Pennsylvania State University, University Park, PA 16802, USA
    Structure 20:1519-27. 2012
  5. pmc Functional identification of the general acid and base in the dehydration step of indole-3-glycerol phosphate synthase catalysis
    Margot J Zaccardi
    From the Department of Chemistry, The Pennsylvania State University, University Park, Pennsylvania 16802
    J Biol Chem 288:26350-6. 2013
  6. ncbi request reprint Amino acid networks in a (β/α)₈ barrel enzyme change during catalytic turnover
    Jennifer M Axe
    Department of Chemistry, The Pennsylvania State University, University Park, Pennsylvania 16802, United States
    J Am Chem Soc 136:6818-21. 2014
  7. doi request reprint Long-range interactions in the α subunit of tryptophan synthase help to coordinate ligand binding, catalysis, and substrate channeling
    Jennifer M Axe
    Department of Chemistry, Pennsylvania State University, 240 Chemistry Building, University Park, PA 16802, USA
    J Mol Biol 425:1527-45. 2013
  8. pmc Loop-loop interactions govern multiple steps in indole-3-glycerol phosphate synthase catalysis
    Margot J Zaccardi
    Department of Chemistry, The Pennsylvania State University, University Park, Pennsylvania, 16802
    Protein Sci 23:302-11. 2014
  9. doi request reprint Differences in the catalytic mechanisms of mesophilic and thermophilic indole-3-glycerol phosphate synthase enzymes at their adaptive temperatures
    Margot J Zaccardi
    Department of Chemistry, The Pennsylvania State University, University Park, PA 16802, USA
    Biochem Biophys Res Commun 418:324-9. 2012
  10. doi request reprint During transitions proteins make fleeting bonds
    David D Boehr
    Department of Chemistry, The Pennsylvania State University, University Park, PA 16802, USA
    Cell 139:1049-51. 2009

Collaborators

Detail Information

Publications10

  1. pmc Long-range interaction networks in the function and fidelity of poliovirus RNA-dependent RNA polymerase studied by nuclear magnetic resonance
    Xiaorong Yang
    Department of Chemistry, The Pennsylvania State University, University Park, PA 16802, USA
    Biochemistry 49:9361-71. 2010
    ..Mutation of Gly64 results in structural and/or dynamic changes to the network that may affect polymerase fidelity...
  2. doi request reprint Promiscuity in protein-RNA interactions: conformational ensembles facilitate molecular recognition in the spliceosome: conformational diversity in U2AF⁶⁵ facilitates binding to diverse RNA sequences
    David D Boehr
    Department of Chemistry, The Pennsylvania State University, 240 Chemistry Building, University Park, PA, USA
    Bioessays 34:174-80. 2012
    ..Similar binding pathways in other systems have important consequences in biological regulation, molecular evolution, and information storage...
  3. pmc The role of dynamic conformational ensembles in biomolecular recognition
    David D Boehr
    Department of Chemistry, The Pennsylvania State University, University Park, Pennsylvania, USA
    Nat Chem Biol 5:789-96. 2009
    ....
  4. pmc Motif D of viral RNA-dependent RNA polymerases determines efficiency and fidelity of nucleotide addition
    Xiaorong Yang
    Department of Chemistry, The Pennsylvania State University, University Park, PA 16802, USA
    Structure 20:1519-27. 2012
    ..We conclude that motif D of RdRps and, by inference, RTs is the functional equivalent to the fidelity helix of other polymerases...
  5. pmc Functional identification of the general acid and base in the dehydration step of indole-3-glycerol phosphate synthase catalysis
    Margot J Zaccardi
    From the Department of Chemistry, The Pennsylvania State University, University Park, Pennsylvania 16802
    J Biol Chem 288:26350-6. 2013
    ....
  6. ncbi request reprint Amino acid networks in a (β/α)₈ barrel enzyme change during catalytic turnover
    Jennifer M Axe
    Department of Chemistry, The Pennsylvania State University, University Park, Pennsylvania 16802, United States
    J Am Chem Soc 136:6818-21. 2014
    ..These findings demonstrate that amino acid networks, similar to those studied here, are likely important for coordinating structural changes necessary for enzyme function and regulation. ..
  7. doi request reprint Long-range interactions in the α subunit of tryptophan synthase help to coordinate ligand binding, catalysis, and substrate channeling
    Jennifer M Axe
    Department of Chemistry, Pennsylvania State University, 240 Chemistry Building, University Park, PA 16802, USA
    J Mol Biol 425:1527-45. 2013
    ..During catalytic turnover, the protein becomes more rigid on the millisecond timescale and the active-site dynamics are driven to a faster nanosecond timescale...
  8. pmc Loop-loop interactions govern multiple steps in indole-3-glycerol phosphate synthase catalysis
    Margot J Zaccardi
    Department of Chemistry, The Pennsylvania State University, University Park, Pennsylvania, 16802
    Protein Sci 23:302-11. 2014
    ....
  9. doi request reprint Differences in the catalytic mechanisms of mesophilic and thermophilic indole-3-glycerol phosphate synthase enzymes at their adaptive temperatures
    Margot J Zaccardi
    Department of Chemistry, The Pennsylvania State University, University Park, PA 16802, USA
    Biochem Biophys Res Commun 418:324-9. 2012
    ....
  10. doi request reprint During transitions proteins make fleeting bonds
    David D Boehr
    Department of Chemistry, The Pennsylvania State University, University Park, PA 16802, USA
    Cell 139:1049-51. 2009
    ..2009) show that transient hydrogen bonds are critical to the conformational transition of the nitrogen regulatory protein NtrC between its native state and its active state...